Evidence map›Paper›PMID 20304799›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Broad specificity AhpC-like peroxiredoxin and its thioredoxin reductant in the sparse antioxidant defense system of Treponema pallidum.

Derek Parsonage, Daniel C Desrosiers, Karsten R O Hazlett, Yongcheng Sun, Kimberly J Nelson, David L Cox, Justin D Radolf, Leslie B Poole

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.9field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
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  7. Review
  8. Peroxiredoxin Catalysis at Atomic Resolution.Structure (London, England : 1993) · 2016
    Article
  9. Dioxygen and nitric oxide scavenging by Treponema denticola flavodiiron protein: a mechanistic paradigm for catalysis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Derek ParsonageDepartment of Biochemistry, Wake Forest University School of Medicine, Winston-Salem, NC 27157, USA.
Daniel C Desrosiers
Karsten R O Hazlett
Yongcheng Sun
Kimberly J Nelson
David L Cox
Justin D Radolf
Leslie B Poole
Wake Forest University · USCenters for Disease Control and Prevention · USUConn Health · US

Funding

Treponema pallidum Outer Membrane Proteins and Transition Metal AcquisitionR01AI026756 · NIAID · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI RADOLF, JUSTIN D · 1992 to 2017
$5.1M
Mechanistic Studies of Alkyl Hydroperoxide Reductase and Related Redox SystemsR01GM050389 · NIGMS · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI POOLE, LESLIE B · 1994 to 2013
$4.8M
NIAID NIH HHS R01 AI026756NIGMS NIH HHS R01 GM050389
6 · The paper itself

Abstract

Little is known about the mechanisms by which Treponema pallidum (Tp), the causative agent of syphilis, copes with oxidative stress as it establishes persistent infection within its obligate human host. The Tp genomic sequence indicates that the bacterium's antioxidant defenses do not include glutathione and are limited to just a few proteins, with only one, TP0509, offering direct defense against peroxides. Although this Tp peroxiredoxin (Prx) closely resembles AhpC-like Prxs, Tp lacks AhpF, the typical reductant for such enzymes. Functionally, TpAhpC resembles largely eukaryotic, nonAhpC typical 2-Cys Prx proteins in using thioredoxin (Trx, TP0919) as an efficient electron donor and exhibiting broad specificity toward hydroperoxide substrates. Unlike many of the eukaryotic Prxs, however, TpAhpC is relatively resistant to inactivation during turnover with hydroperoxide substrates. As is often observed in typical 2-Cys Prxs, TpAhpC undergoes redox-sensitive oligomer formation. Quantitative immunoblotting revealed that TpTrx and TpAhpC are present at very high levels (over 100 and 300 microM, respectively) in treponemes infecting rabbit testes; their redox potentials, at -242 +/- 1 and -192 +/- 2 mV, respectively, are consistent with the role of TpTrx as the cellular reductant of TpAhpC. Transcriptional analysis of select antioxidant genes confirmed the presence of high mRNA levels for ahpC and trx which diminish greatly when spirochetes replicate under in vitro growth conditions. Thus, T. pallidum has evolved an extraordinarily robust, broad-spectrum AhpC as its sole mechanism for peroxide defense to combat this significant threat to treponemal growth and survival during infection.

Indexed as

Amino Acid SequenceAnimalsAntioxidantsGenome, BacterialMolecular Sequence DataOxidation-ReductionPeroxiredoxinsRabbitsSequence AlignmentSubstrate SpecificityThioredoxinsTranscription, GeneticTreponema pallidumAntioxidantsPeroxiredoxinsThioredoxins

Identifiers

PMID20304799
PMCPMC2851974
OpenAlexW1995912615

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.